Analysis of abrB Mutations, Mutant Proteins, and Why abrB Does Not Utilize a Perfect Consensus in the −35 Region of Its σA Promoter
| ISSN: | 0021-9258 |
|---|---|
| Přístupová URL adresa: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12f16bf308df31f22b70adabeb39f5ce https://doi.org/10.1074/jbc.271.5.2621 |
| Rights: | OPEN |
| Přírůstkové číslo: | edsair.doi.dedup.....12f16bf308df31f22b70adabeb39f5ce |
| Autor: | Ke Xu, Mark A. Strauch, Delbert Clark |
| Rok vydání: | 1996 |
| Předmět: |
DNA
Bacterial Molecular Sequence Data Mutant Plasma protein binding Biology medicine.disease_cause Biochemistry chemistry.chemical_compound Bacterial Proteins Sequence Homology Nucleic Acid medicine Amino Acid Sequence Promoter Regions Genetic Molecular Biology Gene Peptide sequence Genetics Mutation Base Sequence fungi Promoter Cell Biology Stop codon DNA-Binding Proteins chemistry DNA Bacillus subtilis Protein Binding Transcription Factors |
| Zdroj: | Journal of Biological Chemistry. 271:2621-2626 |
| ISSN: | 0021-9258 |
| Popis: | The Bacillus subtilis global regulator AbrB is a DNA-binding protein composed of six identical monomers of 96 amino acids that shows specificity to the promoter regions of its target genes including its own. We have sequenced thirteen previously uncharacterized abrB mutations. Four mutant AbrB proteins were purified, and their DNA-binding properties and multimeric structures were examined. AbrB23 (R25S) had no appreciable DNA binding activity but retained a hexameric structure, indicating that Arg25 is important in DNA interactions. Three other mutant proteins, AbrB1 (C56Y), AbrB19 (Gln83-->termination codon), and AbrB100 (L69P), showed decreased DNA binding and altered multimeric interactions. Analysis of the expression and AbrB binding affinities of mutant abrB promoters demonstrated that a consensus -35 region is incompatible with proper autoregulation of the abrB gene. |
| Databáze: | OpenAIRE |
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